Bejar Clarisa M, Ballicora Miguel A, Gómez-Casati Diego F, Iglesias Alberto A, Preiss Jack
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
FEBS Lett. 2004 Aug 27;573(1-3):99-104. doi: 10.1016/j.febslet.2004.07.060.
Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by chromatographic procedures. Separate expression of these polypeptides produced inactive unstable forms. All these results indicated that the ADP-glucose pyrophosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability.
